NMT_MSEPV
ID NMT_MSEPV Reviewed; 298 AA.
AC Q9YW20;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Putative glycylpeptide N-tetradecanoyltransferase;
DE EC=2.3.1.97;
DE AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase;
DE Short=NMT;
DE AltName: Full=Peptide N-myristoyltransferase;
GN OrderedLocusNames=MSV072;
OS Melanoplus sanguinipes entomopoxvirus (MsEPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Entomopoxvirinae; Deltaentomopoxvirus.
OX NCBI_TaxID=83191;
OH NCBI_TaxID=65742; Melanoplus sanguinipes (Migratory grasshopper).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Tucson;
RX PubMed=9847359; DOI=10.1128/jvi.73.1.533-552.1999;
RA Afonso C.L., Tulman E.R., Lu Z., Oma E., Kutish G.F., Rock D.L.;
RT "The genome of Melanoplus sanguinipes entomopoxvirus.";
RL J. Virol. 73:533-552(1999).
RN [2]
RP POSSIBLE FUNCTION.
RX PubMed=11955007; DOI=10.1006/jmbi.2002.5425;
RA Maurer-Stroh S., Eisenhaber B., Eisenhaber F.;
RT "N-terminal N-myristoylation of proteins: refinement of the sequence motif
RT and its taxon-specific differences.";
RL J. Mol. Biol. 317:523-540(2002).
CC -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC certain proteins. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) +
CC N-tetradecanoylglycyl-[protein]; Xref=Rhea:RHEA:15521, Rhea:RHEA-
CC COMP:12666, Rhea:RHEA-COMP:12667, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:64723,
CC ChEBI:CHEBI:133050; EC=2.3.1.97;
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
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DR EMBL; AF063866; AAC97628.1; -; Genomic_DNA.
DR PIR; T28233; T28233.
DR RefSeq; NP_048143.1; NC_001993.1.
DR SMR; Q9YW20; -.
DR GeneID; 1449891; -.
DR KEGG; vg:1449891; -.
DR Proteomes; UP000172353; Genome.
DR GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR022676; NMT_N.
DR Pfam; PF01233; NMT; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..298
FT /note="Putative glycylpeptide N-tetradecanoyltransferase"
FT /id="PRO_0000064250"
SQ SEQUENCE 298 AA; 35805 MW; E2F777FC74BD0694 CRC64;
MNYWESKSIC TVFTKYNDTE IINKIDPVKS NIDHSLYKQY TIGYMSNFNI VNICKFVNKH
SNYIFDIDTF SWLVLNPFSD PSFNIVLYDN DKIVATIVGI LRSIKIKNEI HKIIHTTFLT
VDENYRKQGI HFYIIDKLME NAFNKGVLLG IFSTMKKIKK IKCVNVQDTY IIKSDSKKYK
ENNNVFDYKK LNQKNDDLYF IYNDMEIEYW FNKKYCHIIS IYNNLFCFLK IKYKNNENLN
ILIEQYIHNK NINKYSIPNN SIMFSQYIQL PQIKLQNQIY TYIYNLNFNN LKCNICMF